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TitleMolecular understanding of calcium permeation through the open Orai channel.
Journal, issue, pagesPLoS Biol, Vol. 17, Issue 4, Page e3000096, Year 2019
Publish dateApr 22, 2019
AuthorsXiaofen Liu / Guangyan Wu / Yi Yu / Xiaozhe Chen / Renci Ji / Jing Lu / Xin Li / Xing Zhang / Xue Yang / Yuequan Shen /
PubMed AbstractThe Orai channel is characterized by voltage independence, low conductance, and high Ca2+ selectivity and plays an important role in Ca2+ influx through the plasma membrane (PM). How the channel is ...The Orai channel is characterized by voltage independence, low conductance, and high Ca2+ selectivity and plays an important role in Ca2+ influx through the plasma membrane (PM). How the channel is activated and promotes Ca2+ permeation is not well understood. Here, we report the crystal structure and cryo-electron microscopy (cryo-EM) reconstruction of a Drosophila melanogaster Orai (dOrai) mutant (P288L) channel that is constitutively active according to electrophysiology. The open state of the Orai channel showed a hexameric assembly in which 6 transmembrane 1 (TM1) helices in the center form the ion-conducting pore, and 6 TM4 helices in the periphery form extended long helices. Orai channel activation requires conformational transduction from TM4 to TM1 and eventually causes the basic section of TM1 to twist outward. The wider pore on the cytosolic side aggregates anions to increase the potential gradient across the membrane and thus facilitate Ca2+ permeation. The open-state structure of the Orai channel offers insights into channel assembly, channel activation, and Ca2+ permeation.
External linksPLoS Biol / PubMed:31009446 / PubMed Central
MethodsEM (single particle)
Resolution5.6 Å
Structure data

EMDB-9641:
Calcium release-activated calcium channel protein 1, P288L mutant
Method: EM (single particle) / Resolution: 5.6 Å

Source
  • Drosophila (fruit flies)

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